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Determination of protein‐only RNase P interactome in Arabidopsis mitochondria and chloroplasts identifies a complex between PRORP1 and another NYN domain nuclease
Author(s) -
Bouchoucha Ayoub,
Waltz Florent,
Bonnard Géraldine,
Arrivé Mathilde,
Hammann Philippe,
Kuhn Lauriane,
Schelcher Cédric,
Zuber Hélène,
Gobert Anthony,
Giegé Philippe
Publication year - 2019
Publication title -
the plant journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.058
H-Index - 269
eISSN - 1365-313X
pISSN - 0960-7412
DOI - 10.1111/tpj.14458
Subject(s) - rnase mrp , rnase p , biology , exosome complex , arabidopsis , ribonucleoprotein , interactome , rna , protein subunit , microbiology and biotechnology , gene , biochemistry , mutant
Summary The essential type of endonuclease that removes 5′ leader sequences from transfer RNA precursors is called RNase P. While ribonucleoprotein RNase P enzymes containing a ribozyme are found in all domains of life, another type of RNase P called ‘PRORP’, for ‘PROtein‐only RNase P’, is composed of protein that occurs only in a wide variety of eukaryotes, in organelles and in the nucleus. Here, to find how PRORP functions integrate with other cell processes, we explored the protein interaction network of PRORP1 in Arabidopsis mitochondria and chloroplasts. Although PRORP proteins function as single subunit enzymes in vitro , we found that PRORP1 occurs in protein complexes and is present in high‐molecular‐weight fractions that contain mitochondrial ribosomes. The analysis of immunoprecipitated protein complexes identified proteins involved in organellar gene expression processes. In particular, direct interaction was established between PRORP1 and MNU2 a mitochondrial nuclease. A specific domain of MNU2 and a conserved signature of PRORP1 were found to be directly accountable for this protein interaction. Altogether, results revealed the existence of an RNA maturation complex in Arabidopsis mitochondria and suggested that PRORP proteins cooperated with other gene expression factors for RNA maturation in vivo .